cysteine and flavin-adenine dinucleotide

cysteine has been researched along with flavin-adenine dinucleotide in 85 studies

Research

Studies (85)

TimeframeStudies, this research(%)All Research%
pre-199018 (21.18)18.7374
1990's26 (30.59)18.2507
2000's25 (29.41)29.6817
2010's14 (16.47)24.3611
2020's2 (2.35)2.80

Authors

AuthorsStudies
Ohnishi, T; Salerno, JC1
Kenney, WC; Singer, TP2
Prongay, AJ; Williams, CH2
Ahmed, SA; Claiborne, A; Schulz, GE; Stehle, T1
Claiborne, A; Poole, LB1
Kaminsky, LS; Lee, JJ1
Katsume, T; Muratsubaki, H1
Ikeda, Y; Okamura-Ikeda, K; Tanaka, K1
Funaba, T; Izaki, K; Tashiro, Y1
Cronin, JR; Edmondson, DE; Hendriks, R; Kenney, WC; Singer, TP; Walker, WH1
Juchau, MR; Krasner, J; Yaffe, SJ1
Ronchi, S; Williams, CH1
Hayashi, R; Hosomi, S; Mizoguchi, T; Uehara, K; Yonezawa, M1
Kearney, EB; Seng, R; Singer, TP; Walker, WH1
Brumby, PE; Casola, L; Massey, V1
Krauth-Siegel, RL; Schirmer, I; Schirmer, RH; Untucht-Grau, R1
Hopkins, N; Williams, CH2
Williams, CH1
Hidaka, M; Masaki, H; Niimura, Y; Nishino, T; Ohnishi, K; Suzuki, H; Uozumi, T1
Bui, BT; Florentin, D; Izumi, Y; Marquet, A; Ohshiro, T; Yamamoto, M1
Campbell, WH; Dwivedi, UN; Shiraishi, N1
Jorns, MS; Raibekas, AA2
Bichler, V; Brandsch, R; Decker, K; Mauch, L1
Krishna, TS; Kuriyan, J; Waksman, G; Williams, CH1
Claiborne, A; Schulz, GE; Stehle, T1
Cesura, AM; Da Prada, M; Gottowik, J; Lang, G; Malherbe, P1
Brandsch, R; Henninger, HP; Stoltz, M1
Barber, MJ; Quinn, GB; Smith, ET; Trimboli, AJ1
Claiborne, A; Hol, WG; Yeh, JI1
Hirashiki, I; Hiro, I; Ito, A; Ogata, F; Tsugeno, Y1
Gorren, AC; Mayer, B; Schmidt, K; Schrammel, A1
Mulrooney, SB; Williams, CH1
Rao, GR; Sengupta, S; Subbarap Shaila, M1
Mulrooney, SB; Veine, DM; Wang, PF; Williams, CH1
Hu, Z; Poulton, JE1
Amzel, LM; Bianchet, MA; Foster, CE; Talalay, P; Zhao, Q1
Poulsen, LL; Robertus, JD; Suh, JK; Ziegler, DM1
Chen, SG; Monnier, VM; Takahashi, M; Wu, X1
Büchert, T; Fritz, G; Huber, H; Kroneck, PM; Stetter, KO1
Chang, SI; Choi, JD; Chong, CK; Shin, HJ1
Banerjee, A; Dangott, LJ; Fitzpatrick, PF; Gadda, G1
Casey, PJ; Coates, RM; Digits, JA; Pyun, HJ; Tschantz, WR1
Gomes, CM; Lemos, RS; Teixeira, M1
Fujii, J; Fujii, T; Fujiwara, N; Taniguchi, N1
Fass, D; Gross, E; Kaiser, CA; Sevier, CS; Vala, A1
Bardwell, JC; Collet, JF1
Ito, A; Ma, J1
Dick, S; Frey, HE; Lepock, JR; Siemann, S; Viswanatha, T1
Hofhaus, G; Lee, JE; Lisowsky, T; Rosenberg, B; Tews, I1
Dailey, HA; Dailey, TA; Rose, JP; Wang, BC; Wu, CK1
Blaesse, M; Huber, R; Kupke, T; Steinbacher, S1
Munro, AW; Roitel, O; Scrutton, NS1
Kirchner, U; Müller, R; van Berkel, WJ; Westphal, AH1
NAIR, PM; VAIDYANATHAN, CS1
OSAJIMA, Y; YAMAFUJI, K1
LEINWEBER, FJ; MONTY, KJ1
Daff, S1
Green, J; Paget, MS1
Arcari, P; Masullo, L; Masullo, M; Ruggiero, A; Ruocco, MR1
Bruckner, RC; Hassan-Abdallah, A; Jorns, MS; Zhao, G1
Hassan-Abdallah, A; Jorns, MS; Zhao, G1
Drew, DP; Fincher, GB; Lahnstein, J; Lunde, C1
Kutchan, TM; Macheroux, P; Winkler, A1
Bates, JN; Hashmi-Hill, MP; Lewis, SJ; Robertson, TP; Sandock, K1
Inanaga, H; Ito, K; Numata, T; Nureki, O; Osawa, T; Tomita, K1
Chen, CL; Chen, YR; Garg, V; Green-Church, KB; Hu, K; Kang, PT; Zhang, L1
Ali, V; Husain, A; Jeelani, G; Nozaki, T; Sato, D; Soga, T; Suematsu, M1
Dobritzsch, D; Lindqvist, Y; Lohkamp, B; Voevodskaya, N1
Arai, S; Blaber, M; Kurihara, K; Kuroki, R; Morimoto, S; Shoyama, Y; Takeuchi, A; Tamada, T; Taura, F1
Binda, C; Boy-Röttger, S; Buroni, S; Chiarelli, LR; Cole, ST; De Rossi, E; Degiacomi, G; Dhar, N; Dyson, PJ; Edmondson, DE; Fullam, E; Lucarelli, AP; Mattevi, A; McKinney, JD; Molteni, E; Neres, J; Pasca, MR; Pojer, F; Read, RJ; Riccardi, G; Zanoni, G1
Hwang, S; Kim, S; Lazar, P; Lee, KO; Lee, KW; Lee, SY; Lee, Y; Moon, JC; Shon, Y; Thangapandian, S1
Fan, S; Hou, C; Lang, Q; Liu, A1
Ferri, S; Kojima, K; Shiota, M; Sode, K; Tsugawa, W; Yamazaki, T; Yoshimatsu, K1
Capacho, AS; Machuqueiro, M; Teixeira, VH1
Boyd, JM; Carabetta, VJ; Dubnau, D; Krebs, C; Martinie, RJ; Mashruwala, AA; Tanner, AW1
Tao, P; Zhou, H; Zoltowski, BD1
Barbiroli, A; Barile, M; Bonomi, F; Eberini, I; Galluccio, M; Gianazza, E; Iametti, S; Indiveri, C; Leone, P; Tolomeo, M; Vrenna, F1
Shao, W; Wen, B; Xu, L; Yao, P; Zhang, Y; Zheng, W; Zhou, Z; Zhu, G1
Bou-Nader, C; Dozova, N; Hamdane, D; Lacombat, F; Plaza, P1
Campbell, AC; LeBlanc, S; Nam, HG; Schuermann, JP; Sobrado, P; Sultana, N; Tanner, JJ; Valentino, H1
Gudim, I; Hammerstad, M; Hersleth, HP1

Reviews

4 review(s) available for cysteine and flavin-adenine dinucleotide

ArticleYear
Biochemistry of covalently bound flavins.
    Vitamins and hormones, 1974, Volume: 32

    Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acids; Animals; Bacteria; Binding Sites; Chemical Phenomena; Chemistry; Cysteine; Cytochromes; Flavin-Adenine Dinucleotide; Flavins; Histidine; Indoles; Monoamine Oxidase; Mycotoxins; Oxidation-Reduction; Oxidoreductases; Oxidoreductases, N-Demethylating; Protein Binding; Pyrroles; Riboflavin; Succinate Dehydrogenase; Thiamine

1974
Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain.
    European journal of biochemistry, 1981, Volume: 120, Issue:2

    Topics: Amino Acid Sequence; Binding Sites; Cysteine; Dihydrolipoamide Dehydrogenase; Erythrocytes; Flavin-Adenine Dinucleotide; Glutathione Reductase; Humans; NADP; Phosphates; Protein Conformation; Trypsin

1981
Mechanism and structure of thioredoxin reductase from Escherichia coli.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1995, Volume: 9, Issue:13

    Topics: Catalysis; Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Escherichia coli; Flavin-Adenine Dinucleotide; Flavoproteins; Glutathione Reductase; NADP; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary; Structure-Activity Relationship; Thioredoxin-Disulfide Reductase

1995
Bacterial redox sensors.
    Nature reviews. Microbiology, 2004, Volume: 2, Issue:12

    Topics: Bacteria; Bacterial Proteins; Benzoquinones; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Hemeproteins; Iron-Sulfur Proteins; NAD; NADP; Oxidation-Reduction; Oxidative Stress; Signal Transduction

2004

Other Studies

81 other study(ies) available for cysteine and flavin-adenine dinucleotide

ArticleYear
Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: a method of iron quantitation by formation of paramagnetic complexes.
    Biochemical and biophysical research communications, 1976, Dec-06, Volume: 73, Issue:3

    Topics: Binding Sites; Cysteine; Dithionite; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Iron; Iron-Sulfur Proteins; Metalloproteins; Nitric Oxide; Protein Binding; Protein Conformation; Succinate Dehydrogenase; Sulfur

1976
Evidence for a thioether linkage between the flavin and polypeptide chain of Chromatium cytochrome c 552.
    The Journal of biological chemistry, 1977, Jul-25, Volume: 252, Issue:14

    Topics: Acetals; Chemical Phenomena; Chemistry; Chromatium; Cysteine; Cytochrome c Group; Dithionite; Flavin-Adenine Dinucleotide; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Spectrophotometry; Zinc

1977
Oxidation-reduction properties of Escherichia coli thioredoxin reductase altered at each active site cysteine residue.
    The Journal of biological chemistry, 1992, Dec-15, Volume: 267, Issue:35

    Topics: Amino Acid Sequence; Anaerobiosis; Binding Sites; Cysteine; Dithionite; Escherichia coli; Flavin-Adenine Dinucleotide; Mathematics; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Potentiometry; Recombinant Proteins; Spectrophotometry; Thioredoxin-Disulfide Reductase

1992
The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution.
    FEBS letters, 1990, Jul-16, Volume: 267, Issue:2

    Topics: Crystallization; Cysteine; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Models, Molecular; Peroxidases; Protein Conformation; X-Ray Diffraction

1990
Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs.
    The Journal of biological chemistry, 1990, Nov-05, Volume: 265, Issue:31

    Topics: Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Protein Binding; Spectrophotometry; Thioredoxin-Disulfide Reductase

1990
The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid.
    The Journal of biological chemistry, 1989, Jul-25, Volume: 264, Issue:21

    Topics: Amino Acid Sequence; Cysteine; Dithiothreitol; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Isoelectric Focusing; Kinetics; Molecular Sequence Data; NAD; Neurotransmitter Agents; Nitrobenzoates; Oxidation-Reduction; Peptide Fragments; Peroxidases; Protein Denaturation; Spectrophotometry; Sulfhydryl Compounds; Trypsin

1989
Fluorescence probing of the function-specific cysteines of rat microsomal NADPH-cytochrome P-450 reductase.
    Biochemical and biophysical research communications, 1986, Jan-14, Volume: 134, Issue:1

    Topics: Adenine Nucleotides; Animals; Chromatography, High Pressure Liquid; Cysteine; Cytochrome c Group; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluorescence; Male; Microsomes, Liver; NADPH-Ferrihemoprotein Reductase; Rats; Rats, Inbred Strains; Structure-Activity Relationship; Trypsin

1986
Characterization of fumarate reductase from baker's yeast: essential sulfhydryl group for binding of FAD.
    Journal of biochemistry, 1985, Volume: 97, Issue:4

    Topics: Apoenzymes; Cysteine; Dithionitrobenzoic Acid; Flavin-Adenine Dinucleotide; Kinetics; Saccharomyces cerevisiae; Succinate Dehydrogenase

1985
An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria.
    The Journal of biological chemistry, 1985, Jan-25, Volume: 260, Issue:2

    Topics: Acyl-CoA Dehydrogenase, Long-Chain; Amino Acids; Animals; Binding Sites; Chloromercuribenzoates; Cysteine; Ethylmaleimide; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Methylmercury Compounds; Mitochondria, Liver; p-Chloromercuribenzoic Acid; Rats; Spectrophotometry

1985
Mechanism of mercuric chloride resistance in microorganisms. 3. Purification and properties of a mercuric ion reducing enzyme from Escherichia coli bearing R factor.
    Journal of biochemistry, 1974, Volume: 75, Issue:3

    Topics: Ammonium Sulfate; Apoproteins; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Thin Layer; Cysteine; D-Amino-Acid Oxidase; Dithiothreitol; Drug Resistance, Microbial; Escherichia coli; Extrachromosomal Inheritance; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Mercaptoethanol; Mercury; NADP; Spectrophotometry

1974
The covalently bound flavin of Chromatium cytochrome c552. 1. Evidence for cysteine thiohemiacetal at the 8 alpha position.
    European journal of biochemistry, 1974, Oct-02, Volume: 48, Issue:2

    Topics: Acetals; Binding Sites; Chromatium; Cysteine; Cytochromes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Flavins; Molecular Conformation; Protein Binding; Sulfhydryl Compounds

1974
Model systems for aromatic nitro group reduction--relationships to tissue catalyzed reagents.
    Biochemical pharmacology, 1970, Volume: 19, Issue:2

    Topics: Aminobenzoates; Animals; Benzoates; Biological Transport, Active; Blood; Carbon Monoxide; Cysteine; Dialysis; Electrons; Female; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Indicators and Reagents; Liver; Male; Mice; Models, Biological; NAD; NADP; Oxidation-Reduction; Placenta; Pregnancy; Rats; Tissue Extracts

1970
The isolation and primary structure of a peptide containing the oxidation-reduction active cystine of Escherichia coli thioredoxin reductase.
    The Journal of biological chemistry, 1972, Apr-10, Volume: 247, Issue:7

    Topics: Amino Acid Sequence; Amino Acids; Bacterial Proteins; Binding Sites; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Cystine; Disulfides; Electron Transport; Escherichia coli; Flavin-Adenine Dinucleotide; Maleimides; Molecular Weight; NADP; Oxidation-Reduction; Oxidoreductases; Pepsin A; Peptides; Sulfhydryl Compounds; Thiocyanates

1972
Effect of adenine on the riboflavin-sensitized photoreaction. I. Effect of adenine on the photodynamic inactivation of yeast alcohol dehydrogenase in the presence of riboflavin.
    The Journal of vitaminology, 1971, Sep-10, Volume: 17, Issue:3

    Topics: Adenine; Alcohol Oxidoreductases; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Fluoresceins; Methylene Blue; Photochemistry; Riboflavin; Saccharomyces

1971
Sequence and structure of a cysteinyl flavin peptide from monoamine oxidase.
    Biochemical and biophysical research communications, 1971, Jul-16, Volume: 44, Issue:2

    Topics: Amino Acid Sequence; Aminopeptidases; Binding Sites; Chromatography, Paper; Cysteine; Electrophoresis, Paper; Flavin-Adenine Dinucleotide; Fluorometry; Formates; Glycine; Hydrolysis; Indicators and Reagents; Liver; Monoamine Oxidase; Oxidation-Reduction; Peptides; Protein Binding; Serine; Spectrophotometry; Tyrosine

1971
The reversible conversion of lipoyl dehydrogenase to an artifactual enzyme by oxidation of sulfhydryl groups.
    The Journal of biological chemistry, 1966, Nov-10, Volume: 241, Issue:21

    Topics: Catalysis; Chemical Phenomena; Chemistry; Copper; Cysteine; Dihydrolipoamide Dehydrogenase; Flavin-Adenine Dinucleotide; Fluorescence; Sulfhydryl Compounds

1966
Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.
    Biochemistry, 1995, Sep-19, Volume: 34, Issue:37

    Topics: Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NAD; Oxidation-Reduction; Serine; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds

1995
Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides.
    Biochemistry, 1995, Sep-19, Volume: 34, Issue:37

    Topics: Binding Sites; Coloring Agents; Cysteine; Dihydrolipoamide Dehydrogenase; Disulfides; Electron Transport; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; NAD; NADP; Oxidation-Reduction; Phenazines; Serine; Viologens

1995
Role of cysteine 337 and cysteine 340 in flavoprotein that functions as NADH oxidase from Amphibacillus xylanus studied by site-directed mutagenesis.
    The Journal of biological chemistry, 1995, Mar-17, Volume: 270, Issue:11

    Topics: Amino Acid Sequence; Base Sequence; Cysteine; Enzyme Stability; Flavin-Adenine Dinucleotide; Flavoproteins; Gram-Negative Facultatively Anaerobic Rods; Kinetics; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Oligodeoxyribonucleotides; Plasmids; Recombinant Proteins; Restriction Mapping; Spectrophotometry

1995
Stimulatory factors for enzymatic biotin synthesis from dethiobiotin in cell-free extracts of Escherichia coli.
    Bioscience, biotechnology, and biochemistry, 1995, Volume: 59, Issue:5

    Topics: Bacillus; Biotin; Cell Extracts; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Immunosuppressive Agents; NAD; NADP; S-Adenosylmethionine

1995
Generation of multiple mutations in the same sequence via the polymerase chain reaction using a single selection primer.
    Analytical biochemistry, 1994, Volume: 221, Issue:2

    Topics: Base Sequence; Binding Sites; Cysteine; DNA Primers; Escherichia coli; Flavin-Adenine Dinucleotide; Genetic Vectors; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Plasmids; Polymerase Chain Reaction; Recombinant Proteins

1994
Affinity probing of flavin binding sites. 1. Covalent attachment of 8-(methylsulfonyl)FAD to pig heart lipoamide dehydrogenase.
    Biochemistry, 1994, Oct-25, Volume: 33, Issue:42

    Topics: Amino Acid Sequence; Animals; Azotobacter vinelandii; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Dihydrolipoamide Dehydrogenase; Flavin-Adenine Dinucleotide; Molecular Sequence Data; Myocardium; Protein Binding; Spectrophotometry; Swine

1994
Affinity probing of flavin binding sites. 2. Identification of a reactive cysteine in the flavin domain of Escherichia coli DNA photolyase.
    Biochemistry, 1994, Oct-25, Volume: 33, Issue:42

    Topics: Amino Acid Sequence; Binding Sites; Catalysis; Cysteine; Deoxyribodipyrimidine Photo-Lyase; Escherichia coli; Flavin-Adenine Dinucleotide; Molecular Sequence Data; Pyrimidine Dimers; Tetrahydrofolates

1994
Cysteine to serine replacements in 6-hydroxy-D-nicotine oxidase. Consequences for enzyme activity, cofactor incorporation, and formation of high molecular weight protein complexes with molecular chaperones (GroEL).
    The Journal of biological chemistry, 1993, Jun-15, Volume: 268, Issue:17

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Chaperonin 60; Chromatography, Gel; Cysteine; DNA Mutational Analysis; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Heat-Shock Proteins; Molecular Sequence Data; Molecular Weight; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oxidoreductases; Plasmids; Polymerase Chain Reaction; Recombinant Proteins; Serine

1993
Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis.
    Journal of molecular biology, 1994, Feb-25, Volume: 236, Issue:3

    Topics: Amino Acid Sequence; Binding Sites; Computer Graphics; Crystallography, X-Ray; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Models, Molecular; Models, Structural; Molecular Sequence Data; NADP; Oxidation-Reduction; Protein Conformation; Protein Structure, Secondary; Thioredoxin-Disulfide Reductase

1994
NADH binding site and catalysis of NADH peroxidase.
    European journal of biochemistry, 1993, Jan-15, Volume: 211, Issue:1-2

    Topics: Binding Sites; Catalysis; Crystallography; Cysteine; Enterococcus faecalis; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Models, Molecular; NAD; Peroxidases; Protein Structure, Tertiary; X-Ray Diffraction

1993
Characterisation of wild-type and mutant forms of human monoamine oxidase A and B expressed in a mammalian cell line.
    FEBS letters, 1993, Feb-08, Volume: 317, Issue:1-2

    Topics: Cells, Cultured; Cysteine; Flavin-Adenine Dinucleotide; Humans; Isoenzymes; Kinetics; Monoamine Oxidase; Mutagenesis, Site-Directed; Recombinant Fusion Proteins; Transfection

1993
The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD.
    FEBS letters, 1996, May-20, Volume: 386, Issue:2-3

    Topics: Coenzymes; Cysteine; Drug Design; Flavin-Adenine Dinucleotide; Flavins; Histidine; Kinetics; Oxidoreductases; Point Mutation; Structure-Activity Relationship

1996
Thiol modification and site directed mutagenesis of the flavin domain of spinach NADH:nitrate reductase.
    Archives of biochemistry and biophysics, 1996, Jul-01, Volume: 331, Issue:1

    Topics: Amino Acid Sequence; Base Sequence; Circular Dichroism; Cysteine; Enzyme Inhibitors; Ethylmaleimide; Ferricyanides; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction; Spectrophotometry; Spinacia oleracea; Structure-Activity Relationship; Sulfhydryl Reagents

1996
Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution.
    Biochemistry, 1996, Aug-06, Volume: 35, Issue:31

    Topics: Amino Acid Sequence; Binding Sites; Cloning, Molecular; Crystallography, X-Ray; Cysteine; Enterococcus faecalis; Escherichia coli; Flavin-Adenine Dinucleotide; Macromolecular Substances; Models, Molecular; Oxidation-Reduction; Peroxidases; Protein Structure, Secondary; Recombinant Proteins; Sulfenic Acids

1996
Characterization of rat monoamine oxidase A with noncovalently-bound FAD expressed in yeast cells.
    Journal of biochemistry, 1996, Volume: 120, Issue:4

    Topics: Alanine; Animals; Cysteine; DNA, Complementary; Flavin-Adenine Dinucleotide; Kinetics; Kynuramine; Liver; Monoamine Oxidase; Monoamine Oxidase Inhibitors; Mutagenesis, Site-Directed; Pargyline; Protein Binding; Rats; Saccharomyces cerevisiae; Serotonin; Substrate Specificity

1996
Thiols and neuronal nitric oxide synthase: complex formation, competitive inhibition, and enzyme stabilization.
    Biochemistry, 1997, Apr-08, Volume: 36, Issue:14

    Topics: Animals; Arginine; Biopterins; Calmodulin; Cysteine; Dithiothreitol; Enzyme Inhibitors; Enzyme Stability; Flavin-Adenine Dinucleotide; Heme; Mercaptoethanol; NADP; Neurons; Nitric Oxide Synthase; Protein Binding; Rats; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Compounds; Temperature

1997
Evidence for two conformational states of thioredoxin reductase from Escherichia coli: use of intrinsic and extrinsic quenchers of flavin fluorescence as probes to observe domain rotation.
    Protein science : a publication of the Protein Society, 1997, Volume: 6, Issue:10

    Topics: Adenine Nucleotides; Amino Acid Sequence; Binding Sites; Cysteine; Disulfides; Endopeptidases; Escherichia coli; Flavin-Adenine Dinucleotide; Fluorescent Dyes; Kinetics; Mutation; NADP; Peptide Fragments; Protein Conformation; Spectrometry, Fluorescence; Tetradecanoylphorbol Acetate; Thioredoxin-Disulfide Reductase

1997
In vitro and in vivo regulation of assimilatory nitrite reductase from Candida utilis.
    Archives of microbiology, 1997, Volume: 168, Issue:3

    Topics: Ammonium Chloride; Candida; Chloromercuribenzoates; Cysteine; Enzyme Induction; Enzyme Repression; Flavin-Adenine Dinucleotide; Gene Expression Regulation, Enzymologic; Kinetics; NAD; NADP; Nitrite Reductase (NAD(P)H); Nitrite Reductases; p-Chloromercuribenzoic Acid

1997
Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin.
    Protein science : a publication of the Protein Society, 1998, Volume: 7, Issue:6

    Topics: Cysteine; Disulfides; Dithionite; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; NADP; Osmolar Concentration; Oxidation-Reduction; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Structure-Activity Relationship; Sulfhydryl Compounds; Thioredoxin-Disulfide Reductase; Thioredoxins

1998
Molecular analysis of (R)-(+)-mandelonitrile lyase microheterogeneity in black cherry.
    Plant physiology, 1999, Volume: 119, Issue:4

    Topics: Aldehyde-Lyases; Amino Acid Sequence; Base Sequence; Catalytic Domain; Cysteine; DNA Primers; DNA, Complementary; Flavin-Adenine Dinucleotide; Fruit; Gene Expression; Genes, Plant; Glycosylation; Isoenzymes; Molecular Sequence Data; Multigene Family; Protein Sorting Signals; Sequence Homology, Amino Acid

1999
Crystal structure of human quinone reductase type 2, a metalloflavoprotein.
    Biochemistry, 1999, Aug-03, Volume: 38, Issue:31

    Topics: Animals; Binding Sites; Copper; Crystallization; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Flavoproteins; Histidine; Humans; Metalloproteins; Mice; NAD(P)H Dehydrogenase (Quinone); Rats; Solutions; Vitamin K

1999
Lysine 219 participates in NADPH specificity in a flavin-containing monooxygenase from Saccharomyces cerevisiae.
    Archives of biochemistry and biophysics, 1999, Dec-15, Volume: 372, Issue:2

    Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD; NADP; Oxidation-Reduction; Oxygenases; Phosphates; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Alignment; Substrate Specificity

1999
Cloning of amadoriase I isoenzyme from Aspergillus sp.: evidence of FAD covalently linked to Cys342.
    Biochemistry, 2000, Feb-15, Volume: 39, Issue:6

    Topics: Amino Acid Oxidoreductases; Amino Acid Sequence; Aspergillus fumigatus; Base Sequence; Binding Sites; Cloning, Molecular; Cysteine; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Isoenzymes; Molecular Sequence Data; Mutagenesis, Site-Directed; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2000
Adenylylsulfate reductases from archaea and bacteria are 1:1 alphabeta-heterodimeric iron-sulfur flavoenzymes--high similarity of molecular properties emphasizes their central role in sulfur metabolism.
    FEBS letters, 2000, May-04, Volume: 473, Issue:1

    Topics: Adenosine Monophosphate; Amino Acid Motifs; Archaeoglobus fulgidus; Binding Sites; Cysteine; Desulfovibrio; Desulfovibrio vulgaris; Dimerization; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Genes, Bacterial; Iron; Iron-Sulfur Proteins; Models, Molecular; Molecular Weight; Operon; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Sequence Homology, Amino Acid; Spectrophotometry; Sulfur; Sulfur Compounds

2000
Structural and functional role of cysteinyl residues in tobacco acetolactate synthase.
    Biochemical and biophysical research communications, 2000, May-19, Volume: 271, Issue:3

    Topics: Acetolactate Synthase; Cysteine; Disulfides; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Herbicides; Kinetics; Mutagenesis, Site-Directed; Nicotiana; Peptide Fragments; Plants, Toxic; Protein Binding; Protein Conformation; Spectrophotometry; Thiocyanates

2000
Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide.
    The Journal of biological chemistry, 2000, Oct-13, Volume: 275, Issue:41

    Topics: Amino Acid Sequence; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Dioxygenases; Ethylmaleimide; Flavin-Adenine Dinucleotide; Flavoproteins; Fusarium; Half-Life; Kinetics; Mass Spectrometry; Molecular Sequence Data; Oxygenases; Peptide Fragments; Peptide Mapping; Sequence Analysis, Protein; Trypsin; Valerates

2000
Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.
    The Journal of biological chemistry, 2001, Jan-26, Volume: 276, Issue:4

    Topics: Carbon-Sulfur Lyases; Cysteine; Farnesol; Flavin-Adenine Dinucleotide; Hydrogen Peroxide; Lysosomes; Models, Chemical; Sulfides

2001
Acidianus ambivalens Complex II typifies a novel family of succinate dehydrogenases.
    Biochemical and biophysical research communications, 2001, Feb-16, Volume: 281, Issue:1

    Topics: Amino Acid Sequence; Benzoquinones; Cell Membrane; Cysteine; Electron Spin Resonance Spectroscopy; Electron Transport Complex II; Electrophoresis, Polyacrylamide Gel; Flavin-Adenine Dinucleotide; Iron; Models, Biological; Molecular Sequence Data; Multienzyme Complexes; Oxidation-Reduction; Oxidoreductases; Oxygen; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Succinate Dehydrogenase; Sulfhydryl Compounds; Sulfolobaceae; Sulfur; Ultraviolet Rays

2001
Roles of N-terminal active cysteines and C-terminal cysteine-selenocysteine in the catalytic mechanism of mammalian thioredoxin reductase.
    Journal of biochemistry, 2001, Volume: 129, Issue:5

    Topics: Animals; Baculoviridae; Catalysis; COS Cells; Cysteine; Electron Transport; Flavin-Adenine Dinucleotide; Insecta; Mammals; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Structure, Tertiary; Rats; Selenocysteine; Thioredoxin-Disulfide Reductase; Thioredoxins

2001
A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.
    Nature structural biology, 2002, Volume: 9, Issue:1

    Topics: Amino Acid Motifs; Amino Acid Sequence; Binding Sites; Circular Dichroism; Crystallography, X-Ray; Cysteine; Dimerization; Disulfides; Electron Transport; Flavin-Adenine Dinucleotide; Fungal Proteins; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutation; Oxidoreductases; Oxygen; Pliability; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Subunits; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Structure-Activity Relationship

2002
Disulfides out of thin air.
    Nature structural biology, 2002, Volume: 9, Issue:1

    Topics: Amino Acid Motifs; Bacterial Proteins; Binding Sites; Catalysis; Conserved Sequence; Crystallography, X-Ray; Cysteine; Disulfides; Flavin-Adenine Dinucleotide; Fungal Proteins; Membrane Proteins; Models, Chemical; Oxidoreductases; Oxygen; Protein Disulfide-Isomerases; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Structure-Activity Relationship; Water

2002
Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A.
    Journal of biochemistry, 2002, Volume: 131, Issue:1

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cysteine; Enzyme Stability; Flavin-Adenine Dinucleotide; Humans; Kinetics; Molecular Sequence Data; Monoamine Oxidase; Point Mutation; Protein Conformation; Rats; Substrate Specificity; Tyrosine; Yeasts

2002
Recombinant lysine:N(6)-hydroxylase: effect of cysteine-->alanine replacements on structural integrity and catalytic competence.
    Biochimica et biophysica acta, 2002, Feb-11, Volume: 1594, Issue:2

    Topics: Alanine; Calorimetry, Differential Scanning; Cysteine; Dithionitrobenzoic Acid; Enzyme Stability; Flavin-Adenine Dinucleotide; Hot Temperature; Iopanoic Acid; Kinetics; Mixed Function Oxygenases; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Conformation; Recombinant Proteins

2002
The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre.
    European journal of biochemistry, 2003, Volume: 270, Issue:7

    Topics: Binding Sites; Color; Conserved Sequence; Cysteine; Dimerization; Enzyme Activation; Flavin-Adenine Dinucleotide; Genetic Complementation Test; Mitochondrial Proteins; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases Acting on Sulfur Group Donors; Protein Structure, Tertiary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Serine; Spectrophotometry; Structure-Activity Relationship

2003
The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase.
    Protein science : a publication of the Protein Society, 2003, Volume: 12, Issue:5

    Topics: Amino Acid Sequence; Animals; Crystallography, X-Ray; Cysteine; Dithiothreitol; Flavin-Adenine Dinucleotide; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Protein Conformation; Protein Structure, Quaternary; Proteins; Rats; Sequence Alignment

2003
Structure of MrsD, an FAD-binding protein of the HFCD family.
    Acta crystallographica. Section D, Biological crystallography, 2003, Volume: 59, Issue:Pt 8

    Topics: Bacterial Proteins; Bacteriocins; Binding Sites; Carboxy-Lyases; Catalysis; Crystallography, X-Ray; Cysteine; Electrons; Escherichia coli; Flavin-Adenine Dinucleotide; Flavins; Flavoproteins; Models, Chemical; Models, Molecular; Oxygen; Peptides; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary

2003
Electron transfer in flavocytochrome P450 BM3: kinetics of flavin reduction and oxidation, the role of cysteine 999, and relationships with mammalian cytochrome P450 reductase.
    Biochemistry, 2003, Sep-16, Volume: 42, Issue:36

    Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Bacterial Proteins; Binding Sites; Cysteine; Cytochrome P-450 Enzyme System; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Flavins; Humans; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP; NADPH-Ferrihemoprotein Reductase; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry

2003
Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD.
    The Journal of biological chemistry, 2003, Nov-28, Volume: 278, Issue:48

    Topics: Amino Acid Sequence; Archaeoglobus fulgidus; Bacillus; Catalysis; Catechols; Chromatography, High Pressure Liquid; Cysteine; Dimerization; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Mixed Function Oxygenases; Models, Chemical; Models, Molecular; Molecular Sequence Data; NAD; Phenol; Plasmids; Protein Binding; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry; Temperature

2003
AN INDOLE OXIDASE ISOLATED FROM THE LEAVES OF TECOMA STANS.
    Biochimica et biophysica acta, 1964, Mar-09, Volume: 81

    Topics: Aldehydes; Bignoniaceae; Chloromercuribenzoates; Chromatography; Copper; Cyanides; Cysteine; Dimercaprol; Dioxygenases; Electron Transport Complex IV; Flavin-Adenine Dinucleotide; Glutathione; Indoles; Ions; Metabolism; Oxazoles; Oximes; Phenanthrolines; Plants; Quinacrine; Quinolines; Research; Sulfhydryl Compounds

1964
REDUCTION OF NITRATE TO AMMONIA BY ENZYMES ISOLATED FROM GREEN ALGAE.
    Enzymologia, 1964, Jun-30, Volume: 27

    Topics: Ammonia; Chlorophyta; Colorimetry; Cysteine; Dialysis; Eukaryota; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Freeze Drying; Hydrogen-Ion Concentration; Hydroxylamines; Nitrates; Nitrites; Oxidoreductases; Renal Dialysis; Research; Spectrophotometry

1964
CYSTEINE BIOSYNTHESIS IN NEUROSPORA CRASSA. I. THE METABOLISM OF SULFITE, SULFIDE, AND CYSTEINESULFINIC ACID.
    The Journal of biological chemistry, 1965, Volume: 240

    Topics: Amino Acids; Cysteine; Flavin-Adenine Dinucleotide; Metabolism; Molecular Biology; Mutation; NADP; Neurospora; Neurospora crassa; Research; Sulfides; Sulfinic Acids; Sulfites

1965
An appraisal of multiple NADPH binding-site models proposed for cytochrome P450 reductase, NO synthase, and related diflavin reductase systems.
    Biochemistry, 2004, Apr-06, Volume: 43, Issue:13

    Topics: Alanine; Bacillus megaterium; Binding Sites; Catalysis; Cysteine; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; NADP; NADPH-Ferrihemoprotein Reductase; Nitric Oxide Synthase; Oxidation-Reduction; Spectrophotometry; Substrate Specificity

2004
A 35 kDa NAD(P)H oxidase previously isolated from the archaeon Sulfolobus solfataricus is instead a thioredoxin reductase.
    Biochimie, 2004, Volume: 86, Issue:12

    Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Archaea; Base Sequence; Binding Sites; Cloning, Molecular; Consensus Sequence; Cysteine; Disulfides; Enzyme Stability; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; Molecular Weight; Mutation; NADH, NADPH Oxidoreductases; NADPH Oxidases; Sequence Homology, Amino Acid; Sulfolobus solfataricus; Temperature; Thioredoxin-Disulfide Reductase

2004
Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein.
    Biochemistry, 2005, May-03, Volume: 44, Issue:17

    Topics: Apoenzymes; Bacillus; Binding Sites; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Mutagenesis; Oxidoreductases, N-Demethylating; Recombinant Proteins; Sarcosine Oxidase; Spectrophotometry

2005
Role of the covalent flavin linkage in monomeric sarcosine oxidase.
    Biochemistry, 2006, Aug-08, Volume: 45, Issue:31

    Topics: Apoproteins; Bacillus; Bacterial Proteins; Catalysis; Cysteine; Flavin-Adenine Dinucleotide; Mutation; Sarcosine Oxidase

2006
Heterologous expression of cDNAs encoding monodehydroascorbate reductases from the moss, Physcomitrella patens and characterization of the expressed enzymes.
    Planta, 2007, Volume: 225, Issue:4

    Topics: Amino Acid Sequence; Ascorbic Acid; Bryopsida; Catalysis; Cysteine; DNA, Complementary; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Kinetics; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Reactive Oxygen Species; Transformation, Bacterial

2007
6-S-cysteinylation of bi-covalently attached FAD in berberine bridge enzyme tunes the redox potential for optimal activity.
    The Journal of biological chemistry, 2007, Aug-17, Volume: 282, Issue:33

    Topics: Cysteine; Flavin-Adenine Dinucleotide; Kinetics; Mutagenesis, Site-Directed; Mutation, Missense; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Plant Proteins; Spectrum Analysis

2007
Flavin adenine dinucleotide may release preformed stores of nitrosyl factors from the vascular endothelium of conscious rats.
    Journal of cardiovascular pharmacology, 2007, Volume: 50, Issue:2

    Topics: Acetylcholine; Animals; Aorta, Thoracic; Cysteine; Endothelium, Vascular; Flavin-Adenine Dinucleotide; Injections, Intravenous; Male; NG-Nitroarginine Methyl Ester; Nitric Oxide; Nitric Oxide Synthase; Nitroprusside; Radioligand Assay; Rats; Rats, Sprague-Dawley; Receptor, Muscarinic M3; S-Nitrosothiols; Vasodilation

2007
Conserved cysteine residues of GidA are essential for biogenesis of 5-carboxymethylaminomethyluridine at tRNA anticodon.
    Structure (London, England : 1993), 2009, May-13, Volume: 17, Issue:5

    Topics: Amino Acid Sequence; Anticodon; Bacteria; Bacterial Proteins; Binding Sites; Catalytic Domain; Conserved Sequence; Cysteine; Flavin-Adenine Dinucleotide; Molecular Sequence Data; RNA, Transfer; Uridine

2009
Peroxynitrite-mediated oxidative modifications of complex II: relevance in myocardial infarction.
    Biochemistry, 2010, Mar-23, Volume: 49, Issue:11

    Topics: Amino Acid Sequence; Animals; Cell Hypoxia; Cyclic N-Oxides; Cysteine; Disulfides; Electron Transport Complex II; Flavin-Adenine Dinucleotide; Humans; Molecular Sequence Data; Molecular Weight; Muscle Cells; Myocardial Infarction; Oxidation-Reduction; Peroxynitrous Acid; Protein Subunits; Rats; Rats, Sprague-Dawley; Tyrosine

2010
Two atypical L-cysteine-regulated NADPH-dependent oxidoreductases involved in redox maintenance, L-cystine and iron reduction, and metronidazole activation in the enteric protozoan Entamoeba histolytica.
    The Journal of biological chemistry, 2010, Aug-27, Volume: 285, Issue:35

    Topics: Amino Acid Sequence; Animals; Antiprotozoal Agents; Catalytic Domain; Cysteine; Entamoeba histolytica; Enzyme Activation; Flavin-Adenine Dinucleotide; Iron; Iron-Sulfur Proteins; Metronidazole; Molecular Sequence Data; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Protozoan Proteins; Substrate Specificity

2010
Insights into the mechanism of dihydropyrimidine dehydrogenase from site-directed mutagenesis targeting the active site loop and redox cofactor coordination.
    Biochimica et biophysica acta, 2010, Volume: 1804, Issue:12

    Topics: Amino Acid Substitution; Animals; Arginine; Catalytic Domain; Cysteine; Dihydrouracil Dehydrogenase (NADP); Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Flavins; Glutamine; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Pyrimidines; Serine; Spectrophotometry; Swine

2010
Structure and function of ∆1-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa.
    Journal of molecular biology, 2012, Oct-12, Volume: 423, Issue:1

    Topics: Animals; Berberine; Cannabis; Carbon Dioxide; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Glutamic Acid; Histidine; Intramolecular Oxidoreductases; Mutation; Protein Structure, Tertiary; Psychotropic Drugs; Structure-Activity Relationship; Tyrosine

2012
Structural basis for benzothiazinone-mediated killing of Mycobacterium tuberculosis.
    Science translational medicine, 2012, Sep-05, Volume: 4, Issue:150

    Topics: Antitubercular Agents; Bacterial Proteins; Crystallography, X-Ray; Cysteine; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Flavoproteins; Fluorescent Dyes; Kinetics; Lysine; Microbial Sensitivity Tests; Microbial Viability; Models, Molecular; Mutagenesis, Site-Directed; Mycobacterium smegmatis; Mycobacterium tuberculosis; Oxidation-Reduction; Oxidoreductases; Protein Structure, Tertiary; Protein Transport; Subcellular Fractions; Thiazines

2012
Comparative molecular modeling study of Arabidopsis NADPH-dependent thioredoxin reductase and its hybrid protein.
    PloS one, 2012, Volume: 7, Issue:9

    Topics: Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Catalytic Domain; Cysteine; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Isoenzymes; Molecular Chaperones; Molecular Dynamics Simulation; Molecular Sequence Data; NADP; Protein Structure, Tertiary; Recombinant Fusion Proteins; Structure-Activity Relationship; Thioredoxin-Disulfide Reductase

2012
Biofuel cell based self-powered sensing platform for L-cysteine detection.
    Analytical chemistry, 2015, Mar-17, Volume: 87, Issue:6

    Topics: Aspergillus; Benzothiazoles; Bioelectric Energy Sources; Copper; Cysteine; Electron Transport; Enzyme Activation; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Glucose; Glucose 1-Dehydrogenase; Oxygen; Sulfonic Acids; Vitamin K 3

2015
An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes.
    Bioelectrochemistry (Amsterdam, Netherlands), 2016, Volume: 112

    Topics: Amino Acid Sequence; Catalytic Domain; Conserved Sequence; Cysteine; Flavin-Adenine Dinucleotide; Glucose 1-Dehydrogenase; Iron; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Sulfur

2016
The role of electrostatics in TrxR electron transfer mechanism: A computational approach.
    Proteins, 2016, Volume: 84, Issue:12

    Topics: Amino Acid Motifs; Coenzymes; Cysteine; Electron Transport; Electrons; Flavin-Adenine Dinucleotide; Humans; Hydrogen-Ion Concentration; Molecular Dynamics Simulation; Monte Carlo Method; Mutation; Oxidation-Reduction; Poisson Distribution; Protein Domains; Protein Structure, Secondary; Selenocysteine; Static Electricity; Thioredoxin Reductase 1; Water

2016
The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S]
    Molecular microbiology, 2017, Volume: 104, Issue:5

    Topics: Bacillus subtilis; Bacterial Proteins; Cysteine; Flavin-Adenine Dinucleotide; Iron-Sulfur Proteins; Oxidation-Reduction; Phosphorylation; Phylogeny; Spores, Bacterial; Transcription Factors

2017
Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations.
    Scientific reports, 2017, 04-20, Volume: 7

    Topics: Algorithms; Amino Acids; Circadian Clocks; Computational Biology; Crystallography, X-Ray; Cysteine; Darkness; Entropy; Flavin-Adenine Dinucleotide; Fungal Proteins; Light; Molecular Dynamics Simulation; Neurospora crassa; Protein Conformation

2017
Bacterial Production, Characterization and Protein Modeling of a Novel Monofuctional Isoform of FAD Synthase in Humans: An Emergency Protein?
    Molecules (Basel, Switzerland), 2018, Jan-06, Volume: 23, Issue:1

    Topics: Catalytic Domain; Cloning, Molecular; Cysteine; Escherichia coli; Flavin-Adenine Dinucleotide; Gene Expression; Humans; Isoenzymes; Kinetics; Models, Molecular; Nucleotidyltransferases; Oxidation-Reduction; Protein Conformation, alpha-Helical

2018
Impacts of Cys392, Asp393, and ATP on the FAD Binding, Photoreduction, and the Stability of the Radical State of Chlamydomonas reinhardtii Cryptochrome.
    Chembiochem : a European journal of chemical biology, 2019, 04-01, Volume: 20, Issue:7

    Topics: Adenosine Triphosphate; Amino Acid Substitution; Aspartic Acid; Chlamydomonas reinhardtii; Cryptochromes; Cysteine; Flavin-Adenine Dinucleotide; Light; Oxidation-Reduction; Protein Binding; Protein Stability

2019
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO.
    Physical chemistry chemical physics : PCCP, 2019, Apr-24, Volume: 21, Issue:17

    Topics: Adenine; Amino Acid Sequence; Bacillus subtilis; Binding Sites; Cysteine; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Models, Molecular; Oxidation-Reduction; Photochemical Processes; Protein Binding; tRNA Methyltransferases; Tyrosine

2019
Structure and function of a flavin-dependent S-monooxygenase from garlic (
    The Journal of biological chemistry, 2020, 08-07, Volume: 295, Issue:32

    Topics: Biopolymers; Cysteine; Disulfides; Flavin-Adenine Dinucleotide; Garlic; Hydrogen Peroxide; Hydroxylation; Kinetics; NADP; Oxidation-Reduction; Oxygenases; Protein Conformation; Structure-Activity Relationship; Substrate Specificity; Sulfinic Acids

2020
The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase.
    Biochemistry, 2020, 12-29, Volume: 59, Issue:51

    Topics: Bacillus cereus; Bacterial Proteins; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Glucosamine; NADP; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Protein Structure, Quaternary; Staphylococcus aureus

2020